Structure of PDB 4d45 Chain H

Receptor sequence
>4d45H (length=254) Species: 158879 (Staphylococcus aureus subsp. aureus N315) [Search protein sequence]
NLENKTYVIMGIANKRSIAFGVAKVLDQLGAKLVFTYRKERSRKELEKLL
EQLNQPEAHLYQIDVQSDEEVINGFEQIGKDVGNIDGVYHSIAFANMEDL
RGRFSETSREGFLLAQDISSYSLTIVAHEAKKLMPEGGSIVATTYLGGEF
AVQNYNVMGVAKASLEANVKYLALDLGPDNIRVNAISAGPIRTLSAKGVG
GFNTILKEIEERAPLKRNVDQVEVGKTAAYLLSDLSSGVTGENIHVDSGF
HAIK
3D structure
PDB4d45 An Ordered Water Channel in Staphylococcus Aureus Fabi: Unraveling the Mechanism of Substrate Recognition and Reduction.
ChainH
Resolution2.15 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y147 Y157 M160 K164 K199
Catalytic site (residue number reindexed from 1) Y145 Y155 M158 K162 K197
Enzyme Commision number 1.3.1.39: enoyl-[acyl-carrier-protein] reductase (NADPH, Re-specific).
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 NAP H G13 A15 S19 I20 R40 K41 D66 V67 S93 I94 A95 T145 T146 Y147 K164 A190 P192 I193 T195 S197 G11 A13 S17 I18 R38 K39 D64 V65 S91 I92 A93 T143 T144 Y145 K162 A188 P190 I191 T193 S195
BS02 J47 H A95 A97 Y147 Y157 M160 S197 A93 A95 Y145 Y155 M158 S195 MOAD: Ki=0.17nM
Gene Ontology
Molecular Function
GO:0000166 nucleotide binding
GO:0004318 enoyl-[acyl-carrier-protein] reductase (NADH) activity
GO:0016491 oxidoreductase activity
GO:0141148 enoyl-[acyl-carrier-protein] reductase (NADPH) activity
Biological Process
GO:0006633 fatty acid biosynthetic process

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Molecular Function
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Biological Process
External links
PDB RCSB:4d45, PDBe:4d45, PDBj:4d45
PDBsum4d45
PubMed25706582
UniProtA0A0J9X1Y0

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